Physical changes in the epsilon prototoxin molecule of Clostridium perfringens during enzymatic activation
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چکیده
منابع مشابه
Physical changes in the epsilon prototoxin molecule of Clostridium perfringens during enzymatic activation.
Enzymatic activation of Clostridium perfringens epsilon prototoxin removed a small basic part of the molecule, causing a slight change in molecular weight (32,700 to 31,200) and a large change in isoelectric point (from pH 8.02 into fractions of 5.36 and 5.74).
متن کاملClostridium perfringens type D epsilon prototoxin. Some chemical, immunological and biological properties of a highly purified prototoxin.
WORTHINGTON, R. W., MOLDERS, MARIAS. G . & VAN RENSBURG, J . J. , 1973. Clostridium perfringens typeD epsilon prototoxin. Some chemical, immunological and biological properties of a highly purified preparation of proto toxin . Onderstepoort J. vet. Res. 40(4) 145152 (1973) Highly purified C/. perfringens typeD epsilon prototoxin was prepared by ammonium sulphate precipitation and DEAE cellulose...
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Purified epsilon prototoxin of Clostridium perfringens type D was produced, purified, and detoxified by the stoiechiometric method of non-radioactive iodine incorporation. Different degrees of iodination were perfomed and the toxicity of the derivatives were analysed by in vivo studies. Toxicity decreased inversely to the iodine incorporation. Eletrophoretic analysis showed different levels of ...
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Fusion protein technology represents the strategy to achieve rapid, efficient, and cost-effective proteinexpression. Epsilon and Beta toxins are the most potent Clostridial toxins and cause disease in animals.This study describes in silico fusion of Clostridium perfringens types D and B epsilon and beta toxin genesthat was used for cloning in E.coli. The etx and cpb genes were...
متن کاملTryptophan content of Clostridium perfringens epsilon toxin.
The tryptophan content of Clostridium perfringens epsilon toxin was investigated. When the tryptophan content was determined by amino acid analysis after the hydrolysis of epsilon prototoxin with methanesulfonic acid containing 3-(2-aminoethyl)indole and by the spectrophotometric method with N-bromosuccinimide, the number of tryptophan residues was calculated at 1/mol of the protein. Cleavage o...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1977
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.18.2.549-551.1977